PDBsum entry: 1prr

Binding protein

PDB id: 1prr

Contents

Protein chain

173 a.a. *

Metals

_CA ×2

* Residue conservation analysis

PDB id:

1prr

Name:

Binding protein

Title:

Nmr-derived three-dimensional solution structure of protein s complexed with calcium

Structure:

Development-specific protein s. Chain: a. Engineered: yes

Source:

Myxococcus xanthus. Organism_taxid: 34

NMR struc:

1 models

Authors:

S.Bagby,T.S.Harvey,S.G.Eagle,S.Inouye,M.Ikura

Key ref:

S.Bagby et al. (1994). NMR-derived three-dimensional solution structure of protein S complexed with calcium. Structure, 2, 107-122. PubMed id: 8081742 DOI: 10.1016/S0969-2126(00)00013-7

Date:

25-Mar-94 Release date: 31-Aug-94

Protein chain

P02966  (DESS_MYXXA) -  Development-specific protein S

Seq: 173 a.a.

Struc: 173 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: sporulation resulting in formation of a cellular spore (1 term)

DOI no: 10.1016/S0969-2126(00)00013-7

Structure 2:107-122 (1994)

PubMed id: 8081742

NMR-derived three-dimensional solution structure of protein S complexed with calcium.

S.Bagby, T.S.Harvey, S.G.Eagle, S.Inouye, M.Ikura.

ABSTRACT

BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.

Selected figure(s)

Figure 2.
Figure 2. Schematic representation of the backbone of protein S, generated using Molscript [35]. Ca ^2+ions are represented by spheres. (b)Stereo view of the C ^αtrace of protein S. Ca ^2+ions are represented by crosses. In both (a) and (b), C ^αatoms of residues at the ends of β -strands and α- helices are labelled. Figure 2. Schematic representation of the backbone of protein S, generated using Molscript [[4]35]. Ca ^2+ions are represented by spheres. (b)Stereo view of the C ^αtrace of protein S. Ca ^2+ions are represented by crosses. In both (a) and (b), C ^αatoms of residues at the ends of β -strands and α- helices are labelled.

Figure 7.
Figure 7. Comparison of the linkers of protein S, γ B- crystallin and β B2-crystallin (in stereo). The overlay was generated by fitting C ^αatoms of residues 87–91 of proteins S (red) and residues 82–86 of β B2-crystallin (blue) to C ^αatoms of residues 82–86 of γ B- crystallin (pale green). The linkers are shown vertically for clarity, with the amino-terminal end at the bottom of the picture. Figure 7. Comparison of the linkers of protein S, γ B- crystallin and β B2-crystallin (in stereo). The overlay was generated by fitting C ^αatoms of residues 87–91 of proteins S (red) and residues 82–86 of β B2-crystallin (blue) to C ^αatoms of residues 82–86 of γ B- crystallin (pale green). The linkers are shown vertically for clarity, with the amino-terminal end at the bottom of the picture.

The above figures are reprinted by permission from Cell Press: Structure (1994, 2, 107-122) copyright 1994.

Figures were selected by an automated process.